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Biochem Lecture 5

Review of Protein Structure

QuestionAnswer
Amino acids are joined by amide linkages called _______ forming linear chains called ______. peptide bonds; polypeptides
The _________ group is covalently attached to the _________ group of the next amino acid. a-Carboxyl group; a-Amino group
What is the byproduct of a peptide bond? H20
Are peptide bonds broken when proteins get denatured? No!
Peptide bonds are in the ______ configuration. TRANS
A ______ residue causes limited flexibility due to it's nitrogen being incorporated into the Pyrrolidine ring Proline
The carboxyl (-C=O) and amino (-NH) groups of thepeptide bond are polar and involved in _______ bonds. Hydrogen
The ending of the name of each amino acid in a chain is changed to ____ except the one at the C-terminus "yl"
The Linear Sequence of Amino Acids linked by peptide bonds that determines 3-D structure and the function of the protein. Primary structure
Localized structures within proteins that are formed from hydrogen bonds between -C=O and -NH of the peptide bond. Secondary structure
In ________ H-bonds are formed between the carbonyl oxygen of a peptide bond and the hydrogen attached to the amide group of a peptide bond that is 4 amino acids away Alpha Helices
In _______ H-bonds are formed between linear regions of the polypeptide Beta Sheets
What are the 2 comformations of Beta Sheets? Parallel and Anti-parallel
What 2 amino acids are often involved in a B turn of a Beta Sheet? Proline and Glycine
_______ make up 50% of most polypeptide chains Loop/Coil
What three super secondary structures are often found in DNA binding proteins? Helix-turn-helix, Zinc finger, Leucine zipper
The 3-D conformation of a protein Tertiary structure
______ interactions are the most important in the folding of the peptide chain. Hydrophobic
Apart from Hydrophobic interactions, what other interactions help to form the tertiary structure of a protein? Hydrogen bonds, ionic bonds (electrostatic interactions), and S-S (disulfide bonds)
What is a domain? Independent folding region that allows 1 protein to have multiple functions. Each domain has a specific function.
Found in proteins that have multiple subunits (multiple polypeptide chains) Quaternary structure
Multiple subunits are held together by _________. noncovalent interactions and/or disulfide bonds
_________ aid in protein folding during synthesis. They also prevent misfolding and protein aggregation Chaperones
_____ is required for chaperones to fold proteins. ATP
What structures do denatured proteins lose? Secondary, Tertiary, quaternary
What can cause denaturization of proteins? pH extremes, temperature, Ionic detergents, Organic solvents, Heavy Metal Ions, and Mechanical Stress.
Created by: chilangberto